ID D2PD39_SULID Unreviewed; 332 AA.
AC D2PD39;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 01-MAY-2013, entry version 20.
DE RecName: Full=Probable methylcobalamin:homocysteine methyltransferase;
DE EC=2.1.1.-;
DE AltName: Full=Methionine synthase;
GN Name=metE; OrderedLocusNames=LD85_1953;
OS Sulfolobus islandicus (strain L.D.8.5 / Lassen #2).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfolobus.
OX NCBI_TaxID=425944;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L.D.8.5 / Lassen #2;
RX PubMed=19435847; DOI=10.1073/pnas.0808945106;
RA Reno M.L., Held N.L., Fields C.J., Burke P.V., Whitaker R.J.;
RT "Biogeography of the Sulfolobus islandicus pan-genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:8605-8610(2009).
CC -!- FUNCTION: Catalyzes the transfer of a methyl group from
CC methylcobalamin and methylcobinamide to homocysteine resulting in
CC methionine formation (By similarity).
CC -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity).
CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de
CC novo pathway.
CC -!- SIMILARITY: Belongs to the vitamin-B12 independent methionine
CC synthase family.
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DR EMBL; CP001731; ADB87609.1; -; Genomic_DNA.
DR RefSeq; YP_003419979.1; NC_013769.1.
DR ProteinModelPortal; D2PD39; -.
DR EnsemblBacteria; ADB87609; ADB87609; LD85_1953.
DR GeneID; 8761787; -.
DR KEGG; sii:LD85_1953; -.
DR HOGENOM; HOG000140559; -.
DR KO; K00549; -.
DR OMA; GINAKLM; -.
DR BioCyc; SISL425944:GHS5-1982-MONOMER; -.
DR UniPathway; UPA00051; -.
DR GO; GO:0003871; F:5-methyltetrahydropteroyltriglutamate-homocysteine S-methyltransferase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009086; P:methionine biosynthetic process; IEA:HAMAP.
DR HAMAP; MF_00288; MetE; 1; -.
DR InterPro; IPR022921; MetE_arc.
DR InterPro; IPR002629; Methionine_synth.
DR Pfam; PF01717; Meth_synt_2; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Complete proteome; Metal-binding;
KW Methionine biosynthesis; Methyltransferase; Transferase; Zinc.
FT METAL 211 211 Zinc (By similarity).
FT METAL 213 213 Zinc (By similarity).
FT METAL 296 296 Zinc (By similarity).
SQ SEQUENCE 332 AA; 38258 MW; E1FBBFC249BFF2C1 CRC64;
MSKLPLLPTT VIGSYPRPKW LRESIRLHKA GKISDEDLQE AFNDAVIAVL KDHYNAGVDV
PTDGEVRRDE MVEFFAERIK GFKFYGPVRV WGTAYYRKPS VVSKIEYKKP MLVDEFTFAK
SVSYTDNLKI TITGPYTIAE WSYNEYYKNK KDLVFDLAKA INQEIKNLVE AGAKIIQIDE
PALHTRREDV SWGVEAVNEA VKGVNAKLVM HICYGEYSFV APYLNELKVD QINFAFKIYN
YKPLELLKRY GFDKELGAGV IDVHNRRIET SEEVANDIRK ILEYFTPEKV WINPDCGLKL
LSRKIAYQKL VSMVEGTKVV REELKRKGYS VD
//
